ID A0A2R8ASN3_9RHOB Unreviewed; 942 AA.
AC A0A2R8ASN3;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Polysulfide reductase chain A {ECO:0000313|EMBL:SPF78990.1};
GN Name=psrA {ECO:0000313|EMBL:SPF78990.1};
GN ORFNames=ALP8811_02924 {ECO:0000313|EMBL:SPF78990.1};
OS Aliiroseovarius pelagivivens.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Aliiroseovarius.
OX NCBI_TaxID=1639690 {ECO:0000313|EMBL:SPF78990.1, ECO:0000313|Proteomes:UP000244911};
RN [1] {ECO:0000313|EMBL:SPF78990.1, ECO:0000313|Proteomes:UP000244911}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8811 {ECO:0000313|EMBL:SPF78990.1,
RC ECO:0000313|Proteomes:UP000244911};
RA Keele B.F.;
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; OMOI01000002; SPF78990.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R8ASN3; -.
DR Proteomes; UP000244911; Unassembled WGS sequence.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd02783; MopB_CT_2; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.30.200.210; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR PANTHER; PTHR43598:SF5; DMSO REDUCTASE CHAIN A; 1.
DR PANTHER; PTHR43598; TUNGSTEN-CONTAINING FORMYLMETHANOFURAN DEHYDROGENASE 2 SUBUNIT B; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000244911}.
FT DOMAIN 18..74
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 914..942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 942 AA; 104822 MW; 57F5E94B42D5205F CRC64;
MMSKPENIQI DTSPPVSDEV RKTTCYMCAC RCGINVHMKD GKVAYIEGNR DHPVNKGVLC
GKGSAGIMQH YAPSRLRAPL KRVGPRGSGE FEEISWDEAL EMAVGWMGPL RNEDPSKLAF
FTGRDQSQSF TSWFAQSYGT PNYAAHGGFC SVNMAAAGIY TMGGAFWEFG QPDWDRTKLF
MLFGVAEDHD SNPIKIGLGK LKERGARVIG VNPIRSGYNA IADEWVGITP GTDGLFILAL
VHELFRAGQV DLNYLSRYTN AGFIVNEEPN TAETGLFLRG ATGKPQVICR ETGKLADYDT
PGVMPDLAAT YRHAGQSHRP VFQLMAERYL SDEYAPDAVA DRTGVSADRI RSIAAELAHV
AFEEEIVLDQ PWTDWKGEKH DKMIGRPVSF HAMRGISAHS NGFQTCRALH VLQILLGSVE
VPGGFRFKPP YPKPYDAHPT PHVGVTVGGP LDGPHLGFVR GPEHLALKED GSPARIDKAF
TWENPMSSHG LMHMVISNAH AGDPYKIDTL FLYMANMAWN SSMNSSEVMR MLTDKDDNGD
YVIPHIIYSD AYSSEMVAYA DLILPDTTYL ERHDCISLLD RPICEADGAA DAIRWPVVEP
DRDVRGFQTV LIQLGVKMGL PGFVNEDGSA KYEDYADYIV NHERRPGVGP LAGWRGEDGN
GKGRGEPNPA QLDKYIENGG FWVNHVPENA SFYKPWNKHY QEWAVKRGIF DVESPYVFSL
YVEPMRKFQL AAEGFGDRQP PDNLREQIGQ TMDPLPIWYE PFENSNVDTD EYPIHALTQR
PMHMYHSWGT QNAWLRQITG KNYLYLPTKI WEEHGFKDGD FATVSSVHGQ ITVPVAHHAG
LNGDTIWTWN AIGKRKGAWA LDEDAPEAKD GFLLNHLISE LQPPKGDGLR WSNSDPITGQ
AAWFDLRVKI EKAETKPAES QPAYPPIKSP VGKGPKTVAR KI
//